TGF-beta 3 Human, Plant Chloroplast-Expressed Recombinant Protein

Description

TGF-beta 3 Human, Plant Chloroplast-Expressed Recombinant Protein is a non-glycosylated, 112 aa (aa 301-412), disulfide-linked homodimer with a 25,425.2 Da  molecular mass.

TGF-beta 3 Human is expressed using a novel Nicotiana tabacum chloroplast expression system which eliminates the risk of contamination from endotoxins or animal pathogens. The protein is provided as a lyophilized powder and includes an optimal buffer for reconstitution.

Application

TGFβ3 is primarily used to promote chondrogenesis, the process by which mesenchymal stem cells (MSCs) differentiate into chondrocytes, which are cartilage forming cells. The main mechanism for bone repair requires cartilage formation which provides a framework for bone growth, making TGFβ3 a promising target therapeutic tool. There is also evidence that due to its role in bone homeostasis, TGFβ3 may be used in a restorative or protective manner against osteoporosis. Many papers focus on TGFβ3 use in conjunction with a scaffolding or hydrogel delivery/support system to support bone and cartilage cell therapies, which is a successful  method of providing targeted and prolonged delivery to the wound site.

Outside of cartilage engineering there are cases of TGβ3 applications in organ repair and wound healing. This is specifically due to its mechanisms in reducing fibrosis, which is the excessive or abnormal deposition of collagen and other extracellular matrix proteins which causes tissue stiffening and loss of function. While not as researched as cartilage regeneration applications, there is demonstration of successful preclinical applications of TGFβ3 in cardiac, liver, and uterine fibrosis prevention. 

Chloroplast Expressed

TGF-beta 3 Human is expressed using plants instead of traditional systems like bacteria or animal cells. By engineering chloroplasts, very high protein yields are achieved directly in the leaves, typically in the range of 2 to 5 g/kg. The approach is naturally scalable because the plants are genetically stable, meaning production can be increased simply by growing more plants from seed without the need for bioreactors or complex infrastructure. It is also a safer production method, as avoiding microbial and animal cell systems eliminates the risk of contamination from endotoxins or animal pathogens. By combining high yield, safety, and scalability, this approach enables the production of high-quality growth factors in a more accessible and sustainable way.

Specifications

Amino Acid Sequence

ALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHST
VLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS

SDS-PAGE

Single species with expected mass

Frequently Asked Questions (FAQ)

1. Do you have stability data post-reconstitution (e.g. recommended storage time in solution, freeze–thaw tolerance)?
   • We recommend reconstituting the protein to a final concentration of 0.1–1.0 mg/ml.
   • Following reconstitution, prepare single-use aliquots to minimize repeated freeze–thaw cycles, as these can lead to gradual loss of bioactivity and potential aggregation. Aliquots may be stored at -80 °C for longer-term preservation.
   • The protein is supplied carrier protein-free. If you plan to prepare or store aliquots at concentrations below 0.1 mg/ml, we strongly advise adding a carrier protein (typically 0.1–1.0% w/v high-purity BSA or equivalent) to reduce adsorption losses and improve stability.
   • We are currently assessing the stability of the protein in suspension after reconstitution. Based on the data available so far, the reconstituted protein at 1 mg/ml remains active after 6 months of storage at -80 °C when stored as aliquots without exposure to freeze–thaw cycles. We will continue monitoring these samples quarterly and can provide updated data as it becomes available.
2. Any known aggregation or precipitation issues in complex culture media?
   • Aggregation or precipitation may occur if TGF-β family proteins are reconstituted directly in physiological or neutral pH buffers.
   • We therefore recommend reconstituting the protein in the provided buffer (20% ethanol, 0.12% acetic acid, pH 4.0) at a final concentration of 0.1–1.0 mg/ml.  Alternatively, 4 mM HCl may be used. These mildly acidic conditions help maintain solubility and structural integrity. Again, when working at final concentrations below 0.1 mg/ml, consider adding a carrier protein (e.g. BSA) if compatible with your application.
   • In our assays, we have not observed precipitation or aggregation when the protein is introduced into complex culture media following this approach.
3. Is there a validated shelf life (in months) at −20 °C / −80 °C for the lyophilized product?
   • The lyophilized product has been verified to remain stable for up to 1 year when stored at -80 °C. Stability beyond this period has not yet been formally evaluated; therefore, 1 year is the currently validated shelf life based on available data.
   • Stability studies at -20 °C have not yet been completed, and we therefore recommend storage at -80 °C for long-term preservation.

Usage

This product is intended for laboratory research use only. Not for use in diagnostic or therapeutic procedures. This product may not be used as a pharmaceutical or veterinary drug, agricultural product, or food additive.

• Product Datasheet (PDS)

Synonyms

Transforming Growth Factor beta 3, Transforming Growth Factor-β3, TGFB3, TGF-B3, TGF-β3, TGFβ3, TGF-beta-3, TGF-β-3